1fov: Difference between revisions

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[[Image:1fov.gif|left|200px]]<br /><applet load="1fov" size="350" color="white" frame="true" align="right" spinBox="true"
[[Image:1fov.gif|left|200px]]
caption="1fov" />
 
'''GLUTAREDOXIN 3 FROM ESCHERICHIA COLI IN THE FULLY OXIDIZED FORM'''<br />
{{Structure
|PDB= 1fov |SIZE=350|CAPTION= <scene name='initialview01'>1fov</scene>
|SITE=  
|LIGAND=  
|ACTIVITY=  
|GENE=  
}}
 
'''GLUTAREDOXIN 3 FROM ESCHERICHIA COLI IN THE FULLY OXIDIZED FORM'''
 


==Overview==
==Overview==
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==About this Structure==
==About this Structure==
1FOV is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1FOV OCA].  
1FOV is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1FOV OCA].  


==Reference==
==Reference==
NMR structure of oxidized glutaredoxin 3 from Escherichia coli., Nordstrand K, Sandstrom A, Aslund F, Holmgren A, Otting G, Berndt KD, J Mol Biol. 2000 Oct 27;303(3):423-32. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=11031118 11031118]
NMR structure of oxidized glutaredoxin 3 from Escherichia coli., Nordstrand K, Sandstrom A, Aslund F, Holmgren A, Otting G, Berndt KD, J Mol Biol. 2000 Oct 27;303(3):423-32. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/11031118 11031118]
[[Category: Escherichia coli]]
[[Category: Escherichia coli]]
[[Category: Single protein]]
[[Category: Single protein]]
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[[Category: cis pro 53]]
[[Category: cis pro 53]]


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Revision as of 12:11, 20 March 2008

File:1fov.gif


PDB ID 1fov

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GLUTAREDOXIN 3 FROM ESCHERICHIA COLI IN THE FULLY OXIDIZED FORM


OverviewOverview

A high precision NMR structure of oxidized glutaredoxin 3 [C65Y] from Escherichia coli has been determined. The conformation of the active site including the disulphide bridge is highly similar to those in glutaredoxins from pig liver and T4 phage. A comparison with the previously determined structure of glutaredoxin 3 [C14S, C65Y] in a complex with glutathione reveals conformational changes between the free and substrate-bound form which includes the sidechain of the conserved, active site tyrosine residue. In the oxidized form this tyrosine is solvent exposed, while it adopts a less exposed conformation, stabilized by hydrogen bonds, in the mixed disulfide with glutathione. The structures further suggest that the formation of a covalent linkage between glutathione and glutaredoxin 3 is necessary in order to induce these structural changes upon binding of the glutathione peptide. This could explain the observed low affinity of glutaredoxins for S-blocked glutathione analogues, in spite of the fact that glutaredoxins are highly specific reductants of glutathione mixed disulfides.

About this StructureAbout this Structure

1FOV is a Single protein structure of sequence from Escherichia coli. Full crystallographic information is available from OCA.

ReferenceReference

NMR structure of oxidized glutaredoxin 3 from Escherichia coli., Nordstrand K, Sandstrom A, Aslund F, Holmgren A, Otting G, Berndt KD, J Mol Biol. 2000 Oct 27;303(3):423-32. PMID:11031118

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